Results 61 to 70 of about 207,281 (307)

A Comparison of Pathophysiology in Humans and Rodent Models of Subarachnoid Hemorrhage

Frontiers in Molecular Neuroscience, 2018
Non-traumatic subarachnoid hemorrhage (SAH) affects an estimated 30,000 people each year in the United States, with an overall mortality of ~30%. Most cases of SAH result from a ruptured intracranial aneurysm, require long hospital stays, and result in ...
Jenna L. Leclerc, Jenna L. Leclerc, Joshua M. Garcia, Matthew A. Diller, Anne-Marie Carpenter, Pradip K. Kamat, Brian L. Hoh, Brian L. Hoh, Sylvain Doré, Sylvain Doré, Sylvain Doré   +10 more
doaj   +1 more source

Dual role of heme iron in cancer; promotor of carcinogenesis and an inducer of tumour suppression

, 2021
PURPOSE: Heme is a crucial compound for cell survival but is also equipped with the potential to be toxic and carcinogenic to cells. However, with the recent advancement of knowledge regarding ferroptosis, the iron mediated cell death, heme can be ...
Lee, Katherine TW, Lam, Alfred King-Yin, Gopalan, Vinod, Dissabandara, D Lakal O, Gamage, Sujani MK, D. Lakal O. Dissabandara, Sujani M.K. Gamage, Katherine T.W. Lee, Alfred King-Yin Lam, Vinod Gopalan   +9 more
core   +1 more source

A conserved two-component system senses intracellular iron levels and regulates redox balance in Mycobacterium spp.

Microbiology Spectrum
For bacteria, an intricate coordination between sensing and regulating iron levels and managing oxidative stress is required as their levels are tightly interlinked.
Rahul Yadav, Deepak Kumar Saini
doaj   +1 more source

CCS2, an Octatricopeptide-Repeat Protein, Is Required for Plastid Cytochrome c Assembly in the Green Alga Chlamydomonas reinhardtii

Frontiers in Plant Science, 2017
In bacteria and energy generating organelles, c-type cytochromes are a class of universal electron carriers with a heme cofactor covalently linked via one or two thioether bonds to a heme binding site. The covalent attachment of heme to apocytochromes is
Sara G. Cline, Sara G. Cline, Isaac A. Laughbaum, Patrice P. Hamel, Patrice P. Hamel   +4 more
doaj   +1 more source

Heme and immunity: The heme oxygenase dichotomy

Journal of Inorganic Biochemistry
Heme, an iron containing organic ring, is required for a diverse range of biological processes across all forms of life. Although this nutrient is essential, its pro-inflammatory and cytotoxic properties can lead to cellular damage. Heme oxygenase 1 (HO-1) is an endoplasmic reticulum (ER)-anchored enzyme that degrades heme, releasing equimolar amounts ...
Perry, Melissa, Hamza, Iqbal
openaire   +2 more sources

Silk Fibroin Nanofiber–Immobilized Horseradish Peroxidase Enables Continuous Preparation of Injectable Hydrogels With Negligible Residual Enzyme for Drug Delivery

Advanced Materials Technologies, EarlyView.
Overcoming the immunogenicity challenges of enzyme‐mediated crosslinking, a flow‐through reactor utilizing SFNF‐HRP enables the continuous production of injectable hydrogels. This continuous platform ensures homogeneous crosslinking while minimizing residual HRP in the resulting hydrogels.
Ayari Miyawaki, Shinji Sakai
wiley   +1 more source

Resistance of Nitric Oxide Dioxygenase and Cytochrome c Oxidase to Inhibition by Nitric Oxide and Other Indications of the Spintronic Control of Electron Transfer

Biophysica
Heme enzymes that bind and reduce O2 are susceptible to poisoning by NO. The high reactivity and affinity of NO for ferrous heme produces stable ferrous-NO complexes, which in theory should preclude O2 binding and turnover.
Paul R. Gardner
doaj   +1 more source

The GluTR-binding protein is the heme-binding factor for feedback control of glutamyl-tRNA reductase

eLife, 2019
Synthesis of 5-aminolevulinic acid (ALA) is the rate-limiting step in tetrapyrrole biosynthesis in land plants. In photosynthetic eukaryotes and many bacteria, glutamyl-tRNA reductase (GluTR) is the most tightly controlled enzyme upstream of ALA.
Andreas S Richter, Claudia Banse, Bernhard Grimm   +2 more
doaj   +1 more source

Heme Sensor Proteins [PDF]

Journal of Biological Chemistry, 2013
Heme is a prosthetic group best known for roles in oxygen transport, oxidative catalysis, and respiratory electron transport. Recent years have seen the roles of heme extended to sensors of gases such as O2 and NO and cell redox state, and as mediators of cellular responses to changes in intracellular levels of these gases.
Girvan, Hazel M., Munro, Andrew W.
openaire   +2 more sources

Heme sensor proteins sensing both heme and CO [PDF]

, 2021
Heme, a protoporhyrin IX iron complex, is an important component of many proteins necessary for oxygen transfer, storage and activation, as well as for electron transfer. Another group of hemoproteins includes heme sensor proteins.
Andrlová, Dominika
core